Mediated electrochemistry of peroxidases--effects of variations in protein and mediator structures.
The kinetics of a range of ferrocene derivatives with horseradish peroxidase (HRP), cytochrome c peroxidase (CCP) and 3 charge reversal mutants of cytochrome c peroxidase were measured using cyclic voltammetry. Substantial differences in rate constant (100 fold) were observed between HRP and CCP for the same mediator with smaller differences (4-5 fold) for different mediators with the same enzyme. The rate constant did not seem to be dependent on redox potential differences. Cluster analysis is proposed as a way of classifying mediator reactivity.
Sadeghi
S J
SJ
Department of Biochemistry, Imperial College of Science, Technology and Medicine, London, UK.
Gilardi
G
G
Cass
A E
AE
D003578:Cytochrome-c Peroxidase / Q000737:chemistry*; D004563:Electrochemistry; D005296:Ferrous Compounds / Q000737:chemistry; D006735:Horseradish Peroxidase / Q000737:chemistry*; D000075163:Metallocenes; D010084:Oxidation-Reduction; D013329:Structure-Activity Relationship
D005296:Ferrous Compounds; D000075163:Metallocenes; D006735:Horseradish Peroxidase; D003578:Cytochrome-c Peroxidase; C004998:ferrocene